The effect of lipid composition and physical state of phospholipid monolayer on the binding and incorporation of a basic amphipathic peptide from the C-terminal region of the HIV envelope protein gp41

Dirk Trommeshauser, Silke Krol, Lev D. Bergelson, Hans Joachim Galla

Research output: Contribution to journalArticle

Abstract

The interaction of a peptide identical to the carboxy terminal region of the envelope glycoprotein gp41828 of HIV with negatively charged phospholipids in a monolayer was studied by a Wilhelmy film balance. No significant interaction of the peptide with a monolayer composed of pure neutral but a strong affinity to negatively charged phospholipids could be observed. In mixed phospholipid monolayers the binding of the gp41828 is primarily limited by the amount of acidic phospholipids. The physical state of the monolayer is another important parameter for binding. Clustering of negatively charged phospholipids and the surface pressure are crucial. Ca2+ ions strongly interfere with the peptide-lipid interaction up to complete abolishment. The effects observed are dependent on the nature of the acidic lipid. Phosphatidylglycerol was found to be more sensitive than phosphatidylserine. The significance of the results for processes like virus assembly and budding will be discussed. (C) 2000 Elsevier Science Ireland Ltd.

Original languageEnglish
Pages (from-to)83-92
Number of pages10
JournalChemistry and Physics of Lipids
Volume107
Issue number1
DOIs
Publication statusPublished - Sep 1 2000

Keywords

  • Electrostatic interaction
  • Film balance
  • HIV envelope glycoprotein
  • Lipid monolayer
  • Lipid-peptide interaction

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

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